ABEC1_MONDO
ID ABEC1_MONDO Reviewed; 235 AA.
AC Q9TUI7;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=C->U-editing enzyme APOBEC-1;
DE EC=3.5.4.36 {ECO:0000269|PubMed:10373583};
DE AltName: Full=Apolipoprotein B mRNA-editing enzyme 1;
DE AltName: Full=mRNA(cytosine(6666)) deaminase 1;
GN Name=APOBEC1;
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10373583; DOI=10.1093/nar/27.13.2662;
RA Fujino T., Navaratnam N., Jarmuz A., von Haeselaer A., Scott J.;
RT "C-->U editing of apolipoprotein B mRNA in marsupials: identification and
RT characterisation of APOBEC-1 from the American opossum Monodelphus
RT domestica.";
RL Nucleic Acids Res. 27:2662-2671(1999).
CC -!- FUNCTION: Catalytic component of the apolipoprotein B mRNA editing
CC enzyme complex which is responsible for the postranscriptional editing
CC of a CAA codon for Gln to a UAA codon for stop in the APOB mRNA. May
CC also play a role in the epigenetic regulation of gene expression by
CC participating in DNA demethylation. {ECO:0000269|PubMed:10373583}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(6666) in apoB mRNA + H(+) + H2O = NH4(+) +
CC uridine(6666) in apoB mRNA; Xref=Rhea:RHEA:21772, Rhea:RHEA-
CC COMP:13888, Rhea:RHEA-COMP:13889, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:65315,
CC ChEBI:CHEBI:82748; EC=3.5.4.36;
CC Evidence={ECO:0000269|PubMed:10373583};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9Y235};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9Y235};
CC -!- SUBUNIT: Homodimer. Part of the apolipoprotein B mRNA editing complex
CC with A1CF. Interacts with HNRPAB and SYNCRIP.
CC {ECO:0000250|UniProtKB:P41238}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41238}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AB027195; BAA86051.1; -; mRNA.
DR RefSeq; NP_001028154.1; NM_001032982.2.
DR AlphaFoldDB; Q9TUI7; -.
DR SMR; Q9TUI7; -.
DR STRING; 13616.ENSMODP00000022453; -.
DR Ensembl; ENSMODT00000022843; ENSMODP00000022453; ENSMODG00000018004.
DR GeneID; 554187; -.
DR KEGG; mdo:554187; -.
DR CTD; 339; -.
DR eggNOG; ENOG502SNW2; Eukaryota.
DR GeneTree; ENSGT00940000161190; -.
DR HOGENOM; CLU_080056_3_0_1; -.
DR InParanoid; Q9TUI7; -.
DR OMA; MKLYALE; -.
DR OrthoDB; 1246623at2759; -.
DR TreeFam; TF331356; -.
DR BRENDA; 3.5.4.36; 7945.
DR Proteomes; UP000002280; Chromosome 8.
DR Bgee; ENSMODG00000018004; Expressed in extraembryonic membrane and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central.
DR GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
DR GO; GO:0016556; P:mRNA modification; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IEA:Ensembl.
DR GO; GO:0090310; P:negative regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:Ensembl.
DR GO; GO:0090209; P:negative regulation of triglyceride metabolic process; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR041547; APOBEC1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF18774; APOBEC4_like; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; mRNA processing; Reference proteome;
KW Zinc.
FT CHAIN 1..235
FT /note="C->U-editing enzyme APOBEC-1"
FT /id="PRO_0000171744"
FT DOMAIN 10..131
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 62
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
SQ SEQUENCE 235 AA; 28062 MW; B9C8CD75173079B5 CRC64;
MNSKTGPSVG DATLRRRIKP WEFVAFFNPQ ELRKETCLLY EIKWGNQNIW RHSNQNTSQH
AEINFMEKFT AERHFNSSVR CSITWFLSWS PCWECSKAIR KFLDHYPNVT LAIFISRLYW
HMDQQHRQGL KELVHSGVTI QIMSYSEYHY CWRNFVDYPQ GEEDYWPKYP YLWIMLYVLE
LHCIILGLPP CLKISGSHSN QLALFSLDLQ DCHYQKIPYN VLVATGLVQP FVTWR
